Obligatory Requirement of Sulfation for P-Selectin Binding to Human Salivary Gland Carcinoma Acc-M Cells and Breast Carcinoma ZR-75-30 Cells

Qing, Ying; Geng, Jian Guo

doi:10.4049/jimmunol.168.4.1690

Cited by 23 publications

(28 citation statements)

References 35 publications

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“…As previously stated, sulfated moieties function as the key determinant for P-selectin recognition (22,24,25). In agreement with this interpretation, heparin is a highly sulfated linear polysaccharide composed of repeating units of disaccharides (glucuronic or iduronic acid and glucosamine) that are either N-sulfated of N-acetylated.…”

Section: Discussionsupporting

confidence: 59%

“…It has been reported that heparan sulfate-like proteoglycans serve as the ligand for P-selectin, and that ZR-75-30 cells express a large quantity of heparan sulfate-like proteoglycans (22). However, in ZR-75-30 cells, heparan sulfate-like proteoglycans did not contribute to P-selectin binding.…”

Section: Effects Of the Glycoproteins On P-selectin Binding To Breastmentioning

confidence: 71%

“…As documented previously, P-selectin binds to various types of tumor cells, including human breast carcinoma ZR-75-30 cells (22). In the present study, we first examined the interaction of ZR-75-30 cells with recombinant human P-selectin IgG chimera proteins (P-Fc) by flow cytometry.…”

Section: Resultsmentioning

confidence: 99%

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Inhibitory effects of chemically modified heparin on the P-selectin-mediated adhesion of breast cancer cells in vitro

Gao²,

Zheng³

et al. 2009

Mol Med Rep

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Abstract. P-selectin plays a crucial role during hematogenous metastasis, and the blockade of P-selectin binding to its ligand can attenuate metastasis in various tumor models. Heparin or chemically modified heparins with decreased anticoagulant activities exhibit marked inhibitory effects on P-selectinmediated adhesion. Here, we prepared chemically modified heparins with reduced anticoagulant activities and investigated whether they effectively inhibited P-selectin binding to breast cancer cells under static and flow conditions. The results indicated that P-selectin binding to ZR-75-30 cells was attenuated by chemically modified heparins in a sulfationdependent manner under static and flow conditions. Flow cytometric analysis with heparan sulfate-specific monoclonal antibody revealed that heparan sulfate-like proteoglycans on the tumor cell surface were not implicated in this process. Instead, other glycoproteins were found to serve as P-selectin ligands. These findings suggest that further detailed research involving chemically modified heparins with low or no anticoagulant activities is warranted, and that chemically modified heparins should be considered in the treatment of metastatic breast cancer disease, with P-selectin potentially being a good target.

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Section: Discussionsupporting

confidence: 59%

Section: Effects Of the Glycoproteins On P-selectin Binding To Breastmentioning

confidence: 71%

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Inhibitory effects of chemically modified heparin on the P-selectin-mediated adhesion of breast cancer cells in vitro

Gao²,

Zheng³

et al. 2009

Mol Med Rep

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“…We have no data to suggest that these distinct roles of P-selectin in the metastasis are mediated by nucleolin and, in fact, we hypothesize that different P-selectin receptors may mediate different steps in metastasis. Previously published studies suggest that different human tumor cells could have different P-selectin receptors [7,31,37,56,57]. Thus it is likely that each different Pselectin receptors could each mediate a specific P-selectin function in the process of metastasis.…”

Section: Discussionmentioning

confidence: 99%

Cell-surface nucleolin is a signal transducing P-selectin binding protein for human colon carcinoma cells

Reyes‐Reyes

Akiyama

2008

Experimental Cell Research

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We have previously shown that P-selectin binding to Colo-320 human colon carcinoma cells induces specific activation of the α 5 β 1 integrin with a concomitant increase of cell adhesion and spreading on fibronectin substrates in a phosphatidylinositol 3-kinase (PI 3-K) and p38 MAPK-dependent manner. Here, we identified by affinity chromatography and characterized nucleolin as a P-selectin receptor on Colo-320 cells. Nucleolin mAb D3 significantly decreases the Colo-320 cell adhesion to immobilized P-selectin-IgG-Fc. Moreover, nucleolin becomes clustered at the external side of the plasma membrane of living, intact cells when bound to cross-linked P-selectin-IgG-Fc chimeric protein. We have also found P-selectin binding to Colo-320 cells induces tyrosine phosphorylation specifically of cell-surface nucleolin and formation of a signaling complex containing cell surface nucleolin, PI 3-K, and p38 MAPK. Using siRNA approaches, we have found that both P-selectin binding to Colo-320 cells and formation of the P-selectin-mediated p38 MAPK/ PI 3-K signaling complex require nucleolin expression. These results show that nucleolin (or a nucleolin-like protein) is a signaling receptor for P-selectin on Colo-320 cells and suggest a mechanism for linkage of nucleolin to P-selectin-induced signal transduction pathways that regulate the adhesion and the spreading of Colo-320 on fibronectin substrates.

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“…Hydrogen-bonding pattern was analyzed using the HBPLUS program and standard geometric definitions considering the distance and the angle between the hydrogen atom and the acceptor/donor atoms (50). To compute hydrogen bonds, we used, as criteria, 3,9 Å as maximal distance between heavy atoms and 90°as minimal angle between the donor (D) atom, the hydrogen (H) atom, and the acceptor (A) atom (DHA angle), the probability of finding energetically favorable hydrogen bonds being smaller at longer distances or smaller angles (51).…”

Section: Methodsmentioning

confidence: 99%

Molecular Basis of Leukocyte Rolling on PSGL-1

Bernimoulin¹,

Zeng²,

Abbal³

et al. 2003

Journal of Biological Chemistry

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Interactions between the leukocyte adhesion receptor L-selectin and P-selectin glycoprotein ligand-1 play an important role in regulating the inflammatory response by mediating leukocyte tethering and rolling on adherent leukocytes. In this study, we have examined the effect of post-translational modifications of PSGL-1 including Tyr sulfation and presentation of sialylated and fucosylated O-glycans for L-selectin binding. The functional importance of these modifications was determined by analyzing soluble L-selectin binding and leukocyte rolling on CHO cells expressing various glycoforms of PSGL-1 or mutant PSGL-1 targeted at Nterminal Thr or Tyr residues. Simultaneous expression of core-2 ␤1,6-N-acetylglucosaminyltransferase and fucosyltransferase VII was required for optimal L-selectin binding to PSGL-1. Substitution of Thr-57 by Ala but not of Thr-44, strongly decreased L-selectin binding and leukocyte rolling on PSGL-1. Substitution of Tyr by Phe revealed that PSGL-1 Tyr-51 plays a predominant role in mediating L-selectin binding and leukocyte rolling whereas Tyr-48 has a minor role, an observation that contrasts with the pattern seen for the interactions between PSGL-1 and P-selectin where Tyr-48 plays a key role. Molecular modeling analysis of L-selectin and Pselectin interactions with PSGL-1 further supported these observations. Additional experiments showed that core-2 O-glycans attached to Thr-57 were also of critical importance in regulating the velocity and stability of leukocyte rolling. These observations pinpoint the structural characteristics of PSGL-1 that are required for optimal interactions with L-selectin and may be responsible for the specific kinetic and mechanical bond properties of the L-selectin-PSGL-1 adhesion receptorcounterreceptor pair.Selectins play a major role in regulating leukocyte migration in inflammatory lesions by mediating leukocyte rolling along vascular wall at site of inflammation (1-8). L-selectin is expressed by most leukocytes whereas P-selectin and E-selectin expression is induced on activated platelets and/or endothelial cells (1,2,4,5,7,9). E-, P-, and L-selectin function at different although overlapping phases of the inflammatory reaction (10).P-selectin interacts with its major ligand P-selectin glycoprotein ligand-1 (PSGL-1) 1 and supports leukocyte rolling along postcapillary venules at the earliest phase of inflammation (11-13). Several studies have indicated that L-selectin mediates both primary leukocyte-endothelial interactions (14, 15) and secondary interactions between circulating and adherent leukocytes, which both participate in leukocyte recruitment in inflammatory lesions. Secondary interactions are mainly supported by the interaction of PSGL-1 with L-selectin (16 -18).PSGL-1 is a mucin-like glycoprotein expressed as a homodimer on leukocyte microvilli (4, 19 -21). P-selectin binds with relatively high affinity (K d ϳ300 nM) (22) to PSGL-1 by reacting with N-terminal tyrosine sulfate residues and with the sLe x tetrasaccharide determinants presented...

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Obligatory Requirement of Sulfation for P-Selectin Binding to Human Salivary Gland Carcinoma Acc-M Cells and Breast Carcinoma ZR-75-30 Cells

Cited by 23 publications

References 35 publications

Inhibitory effects of chemically modified heparin on the P-selectin-mediated adhesion of breast cancer cells in vitro

Inhibitory effects of chemically modified heparin on the P-selectin-mediated adhesion of breast cancer cells in vitro

Cell-surface nucleolin is a signal transducing P-selectin binding protein for human colon carcinoma cells

Molecular Basis of Leukocyte Rolling on PSGL-1

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